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Jackson Immuno hrp conjugated secondary antibodies
dCIP4 and Wsp inhibit Gbb secretion. A1–D2 , Confocal images of NMJs 6/7 stained for extracellular <t>Gbb-GFP</t> (red) and <t>HRP</t> (blue) in BG57-GAL4 /+ ( A1 , A2 ), BG57-GAL4 / UAS-gbb-GFP ( B1 , B2 ), BG57-GAL4,Df(3L)ED4342 / UAS-gbb-GFP,dcip4 1 ( C1 , C2 ), and BG57-GAL4
Hrp Conjugated Secondary Antibodies, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 92/100, based on 420 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92/100 stars

Images

1) Product Images from "dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal"

Article Title: dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.0256-10.2010

dCIP4 and Wsp inhibit Gbb secretion. A1–D2 , Confocal images of NMJs 6/7 stained for extracellular Gbb-GFP (red) and HRP (blue) in BG57-GAL4 /+ ( A1 , A2 ), BG57-GAL4 / UAS-gbb-GFP ( B1 , B2 ), BG57-GAL4,Df(3L)ED4342 / UAS-gbb-GFP,dcip4 1 ( C1 , C2 ), and BG57-GAL4
Figure Legend Snippet: dCIP4 and Wsp inhibit Gbb secretion. A1–D2 , Confocal images of NMJs 6/7 stained for extracellular Gbb-GFP (red) and HRP (blue) in BG57-GAL4 /+ ( A1 , A2 ), BG57-GAL4 / UAS-gbb-GFP ( B1 , B2 ), BG57-GAL4,Df(3L)ED4342 / UAS-gbb-GFP,dcip4 1 ( C1 , C2 ), and BG57-GAL4

Techniques Used: Staining

2) Product Images from "AP180 Couples Protein Retrieval to Clathrin-Mediated Endocytosis of Synaptic Vesicles"

Article Title: AP180 Couples Protein Retrieval to Clathrin-Mediated Endocytosis of Synaptic Vesicles

Journal: Traffic (Copenhagen, Denmark)

doi: 10.1111/tra.12153

Independent diffusion of SV proteins following nerve stimulation is sustained for long periods following LAP inactivation Third instar larval NMJ preparations from the indicated genotypes were dissected, incubated with FlAsH-EDT 2 and muscle 4 from segment A2 or A3 was exposed to 488-nm-filtered fluorescent light for 5 min. Clap4C; lap = Clap4C; lap 1 /lap sd3 . Following illumination, the larval NMJs were stimulated continuously with high K + (90 m m ) Jan's solution for 5 min (A and B) or 30 min (C and D) or 10 min (E and F). Following nerve stimulation, the larvae were washed rapidly with Ca 2+ -free HL-3 saline and fixed. The NMJs were then stained for a pair of SV proteins Syn and vGlut or Syt1 and CSP. Panels A–D also show HRP-stained NMJs (blue) to mark the neuronal membrane. The stimulation paradigm does not affect SV protein colocalization in wild-type control larval NMJs in which most SV proteins are colocalized although we note that not all SV proteins are fully colocalized even in the wild-type larval NMJs. In contrast, there are more punctate in LAP-inactivated synaptic boutons and SV proteins are often not colocalized in these punctate (arrows). G and H) Following 10 min of stimulation with high K + , nerve terminals were allowed to rest in Ca 2+ -free HL-3 saline for an additional 20 min prior to fixation. Following the resting period, dramatically large punctate can be observed positive for both Syt1 and Syn (arrowheads) in larval NMJs whose LAP is inactivated, while some portions of the punctate within the bouton are positive for only one of the two SV proteins (arrows). The protocol for both control and experimental samples was identical. Scale bars = 10 µm.
Figure Legend Snippet: Independent diffusion of SV proteins following nerve stimulation is sustained for long periods following LAP inactivation Third instar larval NMJ preparations from the indicated genotypes were dissected, incubated with FlAsH-EDT 2 and muscle 4 from segment A2 or A3 was exposed to 488-nm-filtered fluorescent light for 5 min. Clap4C; lap = Clap4C; lap 1 /lap sd3 . Following illumination, the larval NMJs were stimulated continuously with high K + (90 m m ) Jan's solution for 5 min (A and B) or 30 min (C and D) or 10 min (E and F). Following nerve stimulation, the larvae were washed rapidly with Ca 2+ -free HL-3 saline and fixed. The NMJs were then stained for a pair of SV proteins Syn and vGlut or Syt1 and CSP. Panels A–D also show HRP-stained NMJs (blue) to mark the neuronal membrane. The stimulation paradigm does not affect SV protein colocalization in wild-type control larval NMJs in which most SV proteins are colocalized although we note that not all SV proteins are fully colocalized even in the wild-type larval NMJs. In contrast, there are more punctate in LAP-inactivated synaptic boutons and SV proteins are often not colocalized in these punctate (arrows). G and H) Following 10 min of stimulation with high K + , nerve terminals were allowed to rest in Ca 2+ -free HL-3 saline for an additional 20 min prior to fixation. Following the resting period, dramatically large punctate can be observed positive for both Syt1 and Syn (arrowheads) in larval NMJs whose LAP is inactivated, while some portions of the punctate within the bouton are positive for only one of the two SV proteins (arrows). The protocol for both control and experimental samples was identical. Scale bars = 10 µm.

Techniques Used: Diffusion-based Assay, Incubation, Staining

3) Product Images from "Accumulation of rab4GTP in the Cytoplasm and Association with the Peptidyl-Prolyl Isomerase Pin1 during Mitosis"

Article Title: Accumulation of rab4GTP in the Cytoplasm and Association with the Peptidyl-Prolyl Isomerase Pin1 during Mitosis

Journal: Molecular Biology of the Cell

doi:

Released rab4 is not associated with GDI. Equal numbers of interphase (I) and mitotic (M) rab4/HisGDI CHO double transfectants and control rab4 CHO cells were homogenized and fractionated by high speed centrifugation. Cytosol was retrieved and incubated with 50 μl Ni-NTA beads. Beads were washed three times with ice-cold RIPA buffer and boiled in Laemmli sample buffer. Eluted proteins were separated by SDS-PAGE and analyzed by Western blot using the anti Xpress antibody for HisGDI and a rabbit rab4 antibody. Detection was with HRP-labeled secondary antibodies and enhanced chemiluminescence. Quantitation was done using the NIH image software package (A). Mitotic rab4/HisGDI CHO double transfectants were labeled 45 min with 500 μCi/ml 32 P ortho phosphate. Cells were lysed in 1% octylglucoside as described in MATERIALS AND METHODS. Equal aliquots cleared lysate were incubated for 1 h with a GDI antibody (+) or preimmune serum (-) adsorbed to Protein A Sepharose CL-4B and washed 3 times with octylglucoside wash buffer. Washed immunoprecipitates were boiled 5 min with 100 μl 0.5% SDS in PBS and pelleted. Supernatants were used to immunoprecipitate rab4 as described inMATERIALS AND METHODS, resolved on 12.5% SDS PAA mini gels, and analyzed by phosphorimaging (B).
Figure Legend Snippet: Released rab4 is not associated with GDI. Equal numbers of interphase (I) and mitotic (M) rab4/HisGDI CHO double transfectants and control rab4 CHO cells were homogenized and fractionated by high speed centrifugation. Cytosol was retrieved and incubated with 50 μl Ni-NTA beads. Beads were washed three times with ice-cold RIPA buffer and boiled in Laemmli sample buffer. Eluted proteins were separated by SDS-PAGE and analyzed by Western blot using the anti Xpress antibody for HisGDI and a rabbit rab4 antibody. Detection was with HRP-labeled secondary antibodies and enhanced chemiluminescence. Quantitation was done using the NIH image software package (A). Mitotic rab4/HisGDI CHO double transfectants were labeled 45 min with 500 μCi/ml 32 P ortho phosphate. Cells were lysed in 1% octylglucoside as described in MATERIALS AND METHODS. Equal aliquots cleared lysate were incubated for 1 h with a GDI antibody (+) or preimmune serum (-) adsorbed to Protein A Sepharose CL-4B and washed 3 times with octylglucoside wash buffer. Washed immunoprecipitates were boiled 5 min with 100 μl 0.5% SDS in PBS and pelleted. Supernatants were used to immunoprecipitate rab4 as described inMATERIALS AND METHODS, resolved on 12.5% SDS PAA mini gels, and analyzed by phosphorimaging (B).

Techniques Used: Centrifugation, Incubation, SDS Page, Western Blot, Labeling, Quantitation Assay, Software

Rab4 is in a complex with Pin1 in cytosol during mitosis. Equal numbers of interphase and mitotic rab4/HisPin1 CHO double transfectants and rab4 CHO cells (A, B), or rab4S196Q and rab4S196Q/HisPin1 CHO transfectants (B) were homogenized and fractionated by high speed centrifugation. Cytosol was retrieved and incubated with 50 μl Ni-NTA beads. Beads were washed three times with ice-cold RIPA buffer and boiled in Laemmli sample buffer. Eluted proteins were separated by SDS-PAGE and analyzed by Western blot using the Xpress antibody for HisPin1 and a rabbit rab4 antibody. Detection was done with HRP-labeled secondary antibodies and enhanced chemiluminescence and quantitated using the NIH image software package.
Figure Legend Snippet: Rab4 is in a complex with Pin1 in cytosol during mitosis. Equal numbers of interphase and mitotic rab4/HisPin1 CHO double transfectants and rab4 CHO cells (A, B), or rab4S196Q and rab4S196Q/HisPin1 CHO transfectants (B) were homogenized and fractionated by high speed centrifugation. Cytosol was retrieved and incubated with 50 μl Ni-NTA beads. Beads were washed three times with ice-cold RIPA buffer and boiled in Laemmli sample buffer. Eluted proteins were separated by SDS-PAGE and analyzed by Western blot using the Xpress antibody for HisPin1 and a rabbit rab4 antibody. Detection was done with HRP-labeled secondary antibodies and enhanced chemiluminescence and quantitated using the NIH image software package.

Techniques Used: Centrifugation, Incubation, SDS Page, Western Blot, Labeling, Software

4) Product Images from "Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle"

Article Title: Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle

Journal: Genes & Development

doi:

Skp1 is pericentriolar in purified centrosomes and in NIH-3T3 cells. Centrosomes were purified from CHO cells and prepared for immunofluorescence as described (see Materials and Methods). ( A ) Centrosomes spun onto coverslips were fixed in methanol and labeled with mouse monoclonal antibodies against α-tubulin and affinity-purified rabbit antibodies against Skp1, followed by secondary antibodies. Anti-α-tubulin (green); Anti-Skp1 (red). ( B ) Immunoblotting detects Skp1 in a purified centrosome sample. An NIH-3T3 cell lysate (lanes 1,3 ) and a centrosome sample (lanes 2,4 ) were subjected to Western blotting with either affinity-purified anti-Skp1 antibodies (lanes 1,2 ) or rabbit antibodies to γ-tubulin (lanes 3,4 ). Secondary antibody was HRP-conjugated donkey anti-rabbit IgG and bands were detected with ECL reagents as above. Skp1 and γ-tubulin are indicated (arrows). Molecular mass markers are as indicated. ( C ) NIH-3T3 cells fixed in methanol, and labeled using a mouse mAb against γ-tubulin and with rabbit affinity-purified anti-Skp1 antibodies followed by secondary antibodies. Anti-γ-tubulin (green); anti-Skp1 (red). Deconvolution images of centrosomes in cells at different phases of the cell cycle are pictured ( left to right ).
Figure Legend Snippet: Skp1 is pericentriolar in purified centrosomes and in NIH-3T3 cells. Centrosomes were purified from CHO cells and prepared for immunofluorescence as described (see Materials and Methods). ( A ) Centrosomes spun onto coverslips were fixed in methanol and labeled with mouse monoclonal antibodies against α-tubulin and affinity-purified rabbit antibodies against Skp1, followed by secondary antibodies. Anti-α-tubulin (green); Anti-Skp1 (red). ( B ) Immunoblotting detects Skp1 in a purified centrosome sample. An NIH-3T3 cell lysate (lanes 1,3 ) and a centrosome sample (lanes 2,4 ) were subjected to Western blotting with either affinity-purified anti-Skp1 antibodies (lanes 1,2 ) or rabbit antibodies to γ-tubulin (lanes 3,4 ). Secondary antibody was HRP-conjugated donkey anti-rabbit IgG and bands were detected with ECL reagents as above. Skp1 and γ-tubulin are indicated (arrows). Molecular mass markers are as indicated. ( C ) NIH-3T3 cells fixed in methanol, and labeled using a mouse mAb against γ-tubulin and with rabbit affinity-purified anti-Skp1 antibodies followed by secondary antibodies. Anti-γ-tubulin (green); anti-Skp1 (red). Deconvolution images of centrosomes in cells at different phases of the cell cycle are pictured ( left to right ).

Techniques Used: Purification, Immunofluorescence, Labeling, Affinity Purification, Western Blot

A Nedd8-modified form of Cul1 is present at the centrosome. ( A ) NIH-3T3 cells were grown on cover slips, fixed in methanol and labeled with affinity-purified antibodies against the amino-terminal portion of human Cul1 and with human anti-centrosome antiserum, followed by secondary antibodies and Hoechst dye. Cul1 staining is shown at the centrosome at different times in the cell cycle (top three panels). Cells were also stained with anti-centrosome antibody in combination with blocked anti-amino-terminal Cul1 antibodies ( bottom panel). Cells were visualized and photographed as described (see Materials and Methods). ( B ) Cul1 localizes to the midbody. ( Left and middle ) NIH-3T3 cells were grown on coverslips, fixed in methanol, and labeled with affinity-purified rabbit anti-amino-terminal Cul1 antibodies ( left ) or affinity-purified rabbit anti-carboxy-terminal Cul1 antibodies followed by secondary antibodies( middle ). ( Right ) NIH-3T3 cells expressing Myc-tagged Cul1 were fixed as above and labeled with anti-Myc mAb 9E10 followed by secondary antibodies. ( C ) Immunoblotting also demonstrates that Cul1 is present at the centrosome. Samples as indicated: (Lane 1 ) Sf9 cell extract; (lane 2 ) insect cell extract [Hi5] expressing human Cul1; (lane 3 ) NIH-3T3 cell lysate; (lane 4 ) nuclei prepared from CHO cells; and (lane 5 ) centrosomes purified from CHO cells were subjected to Western blotting with affinity-purified rabbit antibodies to the amino-terminal region of Cul1 followed by HRP-conjugated secondary antibodies. Bands were detected using ECL reagents (Amersham). Two forms of Cul1 detected are indicated (arrows). Positions of migration of molecular mass markers are also indicated. Note also that whole-cell lysate from CHO cells gave a similar result as did 3T3 cell lysate (data not shown). ( D ) Immunoblotting demonstrates that Cul1 is NEDD8-modified. Rabbit affinity-purified anti-Cul1 ( left ) and rabbit anti-NEDD8 ( right ) immunoblots of partially purified Xenopus egg extract (lanes 1 ), and immunoprecipitates from the same partially purified extract using control normal mouse serum (lanes 2 ), or mouse anti-Cul1 antibodies (lanes 3 ). Bands were detected using ECL reagents (Amersham). Two forms of Cul1 and positions of migration of molecular mass markers are indicated.
Figure Legend Snippet: A Nedd8-modified form of Cul1 is present at the centrosome. ( A ) NIH-3T3 cells were grown on cover slips, fixed in methanol and labeled with affinity-purified antibodies against the amino-terminal portion of human Cul1 and with human anti-centrosome antiserum, followed by secondary antibodies and Hoechst dye. Cul1 staining is shown at the centrosome at different times in the cell cycle (top three panels). Cells were also stained with anti-centrosome antibody in combination with blocked anti-amino-terminal Cul1 antibodies ( bottom panel). Cells were visualized and photographed as described (see Materials and Methods). ( B ) Cul1 localizes to the midbody. ( Left and middle ) NIH-3T3 cells were grown on coverslips, fixed in methanol, and labeled with affinity-purified rabbit anti-amino-terminal Cul1 antibodies ( left ) or affinity-purified rabbit anti-carboxy-terminal Cul1 antibodies followed by secondary antibodies( middle ). ( Right ) NIH-3T3 cells expressing Myc-tagged Cul1 were fixed as above and labeled with anti-Myc mAb 9E10 followed by secondary antibodies. ( C ) Immunoblotting also demonstrates that Cul1 is present at the centrosome. Samples as indicated: (Lane 1 ) Sf9 cell extract; (lane 2 ) insect cell extract [Hi5] expressing human Cul1; (lane 3 ) NIH-3T3 cell lysate; (lane 4 ) nuclei prepared from CHO cells; and (lane 5 ) centrosomes purified from CHO cells were subjected to Western blotting with affinity-purified rabbit antibodies to the amino-terminal region of Cul1 followed by HRP-conjugated secondary antibodies. Bands were detected using ECL reagents (Amersham). Two forms of Cul1 detected are indicated (arrows). Positions of migration of molecular mass markers are also indicated. Note also that whole-cell lysate from CHO cells gave a similar result as did 3T3 cell lysate (data not shown). ( D ) Immunoblotting demonstrates that Cul1 is NEDD8-modified. Rabbit affinity-purified anti-Cul1 ( left ) and rabbit anti-NEDD8 ( right ) immunoblots of partially purified Xenopus egg extract (lanes 1 ), and immunoprecipitates from the same partially purified extract using control normal mouse serum (lanes 2 ), or mouse anti-Cul1 antibodies (lanes 3 ). Bands were detected using ECL reagents (Amersham). Two forms of Cul1 and positions of migration of molecular mass markers are indicated.

Techniques Used: Modification, Labeling, Affinity Purification, Staining, Expressing, Purification, Western Blot, Migration

Related Articles

Western Blot:

Article Title: AP180 Couples Protein Retrieval to Clathrin-Mediated Endocytosis of Synaptic Vesicles
Article Snippet: .. Western blot Following dilution in SDS sample buffer, proteins were separated by SDS–PAGE, transferred to nitrocellulose and detected using the following antibodies: goat anti-LAP (1:2000); rabbit anti-vGlut (1:10 000, courtesy of Aaron DiAntonio, and this study); mouse anti-Syn (1:200); rabbit anti-Syt1 (1:1000, Noreen Reist); mouse anti-CSP (1:200, DSHB) and rabbit anti-nSyb (1:1000), followed by probing with HRP-conjugated secondary antibodies (1:1000, Jackson Immunoresearch). .. The HRP signal was detected with ECL Plus (GE Healthcare) and imaged on a Chemi Doc XRS+ Imaging System (BioRad).

Article Title: Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle
Article Snippet: .. Western blotting was performed by standard methods using HRP-conjugated secondary antibodies (Jackson Immunoresearch) and enhanced chemiluminescence (ECL) detection reagents (Amersham). .. Antibodies used for blotting were affinity-purified anti-Skp1 antibodies (0.5 μg/ml), rabbit anti-HA-tag (Medical and Biological Laboratories, Nagoya, Japan, 1:100), rabbit anti-γ-tubulin (XGC-1-4, 1:500; ), affinity-purified rabbit anti-amino-terminal Cul1 (∼0.5 μg/ml; ), and rabbit anti-NEDD8 (Alexis Biochemicals, 1:400).

Article Title: The role of prospero homeobox 1 (PROX1) expression in follicular thyroid carcinoma cells
Article Snippet: .. Determining the Prox1 protein levels by western blot Preparation of total protein extracts from whole cells and Western blotting were carried out as previously described using the following antibodies: goat antibody against human Pro2-Gln259 Prox1 (AF2727, R & D Systems, Minneapolis, MN USA) diluted 1:2000 or rabbit anti-human against Prox1 (Cell Signaling #13910) diluted 1:1000 as primary antibodies, followed by a HRP-conjugated secondary antibody: a rabbit anti-goat secondary antibody (Jackson ImmunoResearch Laboratories, Vest Grow, Pa, USA) diluted 1:20,000 or a goat anti-rabbit antibody (DAKO, Carpinteria, CA, USA) diluted 1:5000, depending on the origin of the primary antibody [ ]. .. The primary antibodies had been previously validated for use in Western blot, immunofluorescent and immunohistochemical analyses as the most reliable out of four different antibodies tested to specifically detect the Prox1 protein.

other:

Article Title: Rab GTPase regulation of VEGFR2 trafficking and signaling in endothelial cells
Article Snippet: Primary antibodies include mouse anti-transferrin receptor, mouse anti-EEA1, mouse anti-Rab7a (Abcam, Cambridge, UK), rabbit anti-Cathepsin D (BD Transduction Labs, Erembodegem, Belgium) rabbit anti-pY1175 VEGFR2, rabbit anti-c-Akt, rabbit anti-p42/44 MAPK (Cell Signaling Technology, Danvers, USA), anti-VEGFR2 and anti-TfR antibodies., HRP-conjugated secondary antibodies were from Jackson ImmunoResearch labs (Soham, UK) whilst AlexaFluor-conjugated secondary antibodies were from Invitrogen (Amsterdam, UK).

SDS Page:

Article Title: AP180 Couples Protein Retrieval to Clathrin-Mediated Endocytosis of Synaptic Vesicles
Article Snippet: .. Western blot Following dilution in SDS sample buffer, proteins were separated by SDS–PAGE, transferred to nitrocellulose and detected using the following antibodies: goat anti-LAP (1:2000); rabbit anti-vGlut (1:10 000, courtesy of Aaron DiAntonio, and this study); mouse anti-Syn (1:200); rabbit anti-Syt1 (1:1000, Noreen Reist); mouse anti-CSP (1:200, DSHB) and rabbit anti-nSyb (1:1000), followed by probing with HRP-conjugated secondary antibodies (1:1000, Jackson Immunoresearch). .. The HRP signal was detected with ECL Plus (GE Healthcare) and imaged on a Chemi Doc XRS+ Imaging System (BioRad).

Labeling:

Article Title: Accumulation of rab4GTP in the Cytoplasm and Association with the Peptidyl-Prolyl Isomerase Pin1 during Mitosis
Article Snippet: .. The mouse monoclonal antibody (Xpress) was purchased from Invitrogen (Leek, The Netherlands), and HRP-conjugated secondary antibodies and fluorescently labeled secondary antibodies were from Jackson Immunoresearch labs (Westgrove, PA). ..

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  • 92
    Jackson Immuno hrp conjugated anti rabbit igg
    Association of hnRNP C with polysomes increases from G1 to mitosis. ( A ) MS measurements of members of the hnRNP family. Bar plot represents the logarithmic ratio of normalized MS intensities for M over G1; heatmaps reflect the relative abundance of each protein during mitosis in either ribosome-associated (‘Ribosome’) or total proteome (‘Total’) samples. ( B ) Polysomes were extracted from G1 and M cytoplasmic lysates by ultracentrifugation through a sucrose cushion, and protein content of the lysates and pellets was monitored by immunoblotting using antibodies to hnRNP C, Poly-A binding protein (PABPC1) and Ribosomal protein L26 (RPL26). ( C ) Polysomes were extracted from G1 and M cells by ultracentrifugation through a sucrose gradient, and protein content of each fraction was monitored by immunoblotting using antibodies to Ribosomal protein P0 (RPLP0) and either hnRNP C (top panel) or SRSF1 (bottom panel). The membrane was simultaneously incubated with either pair of antibodies to allow a more direct comparison of protein amounts. 40S, small ribosomal subunit. ( D ) Polysomes were extracted as in (A) and hnRNP C-bound complexes were immunoprecipitated using antibodies to hnRNP C or <t>IgG</t> as control, followed by incubation with biotin-conjugated puromycin to label nascent polypeptide chains. 5% of polysome pellet and 100% of hnRNP C IP were then subjected to immunoblot analysis using anti-hnRNP C and anti-RPL26, as well as <t>streptavidin-HRP.</t>
    Hrp Conjugated Anti Rabbit Igg, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated anti rabbit igg/product/Jackson Immuno
    Average 92 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
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    92
    Jackson Immuno hrp conjugated secondary antibodies
    dCIP4 and Wsp inhibit Gbb secretion. A1–D2 , Confocal images of NMJs 6/7 stained for extracellular <t>Gbb-GFP</t> (red) and <t>HRP</t> (blue) in BG57-GAL4 /+ ( A1 , A2 ), BG57-GAL4 / UAS-gbb-GFP ( B1 , B2 ), BG57-GAL4,Df(3L)ED4342 / UAS-gbb-GFP,dcip4 1 ( C1 , C2 ), and BG57-GAL4
    Hrp Conjugated Secondary Antibodies, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 92/100, based on 420 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated secondary antibodies/product/Jackson Immuno
    Average 92 stars, based on 420 article reviews
    Price from $9.99 to $1999.99
    hrp conjugated secondary antibodies - by Bioz Stars, 2020-07
    92/100 stars
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    99
    Jackson Immuno horseradish peroxidase hrp conjugated anti mouse igg secondary antibody
    A high-throughput assay (EJIPT) utilizing EJC binding to spliced mRNAs to measure splicing in vitro . Splicing reaction mixtures containing biotin-labeled pre-mRNA, 20 μM each compound, splicing extract, and 0.5 mM ATP are assembled by liquid handler in 384-well plates and incubated for 1.5 h at 30°C. Reaction mixtures are then transferred to a NeutrAvidin-coated plate, which captures biotin-labeled RNAs/RNPs postsplicing. Anti-eIF4AIII (3F1) antibody is added to detect splicing-dependent EJC formation on spliced mRNAs. Following a washing step, incubation with an <t>HRP-conjugated</t> anti-mouse <t>IgG</t> secondary antibody, and then addition of chemiluminescent substrate, signals representing eIF4AIII/mRNA complexes are obtained by an automatic plate reader.
    Horseradish Peroxidase Hrp Conjugated Anti Mouse Igg Secondary Antibody, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Jackson Immuno hrp conjugated anti human igg
    Purified TDM is recognized by Mincle. (A) Chemical structure of TDM. α-Mycolate (shown), methoxy-mycolate, and keto-mycolate are the major subclasses of mycolate found in M. tuberculosis TDM. (B and C) Reporter cells were stimulated with the indicated amount of plate-coated TDM (B) or TDB (C). (D) Reporter cells were stimulated with the indicated amount of TDM, methyl α-mycolate (α-mycolate), or methyl keto-mycolate (keto-mycolate). (E) Reporter cells were stimulated with the indicated amount of TDM and TMM. (F) ELISA-based detection of TDM by Mincle-Ig. hIgG1-Fc (Ig), Mincle-Ig, and Dectin2-Ig were incubated with 0.1 nmol/0.32 cm 2 of plate-coated TDM. Bound protein was detected with <t>anti–hIgG-HRP</t> followed by the addition of colorimetric substrate. (G) Effect of trehalose (100 µg/ml), EDTA (10 mM), rat <t>IgG</t> (10 µg/ml), and anti-Mincle mAb (10 µg/ml) on TDM recognition by Mincle-Ig. ELISA-based detection was performed as in E. (H) Reporter cells were stimulated with TDM, which was treated with trehalase as described in Materials and methods. Cells were also stimulated with plate-coated anti-Mincle mAb treated with trehalase as a negative control. All data are means ± SD for triplicate assays and representative results from three independent experiments with similar results are shown.
    Hrp Conjugated Anti Human Igg, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Association of hnRNP C with polysomes increases from G1 to mitosis. ( A ) MS measurements of members of the hnRNP family. Bar plot represents the logarithmic ratio of normalized MS intensities for M over G1; heatmaps reflect the relative abundance of each protein during mitosis in either ribosome-associated (‘Ribosome’) or total proteome (‘Total’) samples. ( B ) Polysomes were extracted from G1 and M cytoplasmic lysates by ultracentrifugation through a sucrose cushion, and protein content of the lysates and pellets was monitored by immunoblotting using antibodies to hnRNP C, Poly-A binding protein (PABPC1) and Ribosomal protein L26 (RPL26). ( C ) Polysomes were extracted from G1 and M cells by ultracentrifugation through a sucrose gradient, and protein content of each fraction was monitored by immunoblotting using antibodies to Ribosomal protein P0 (RPLP0) and either hnRNP C (top panel) or SRSF1 (bottom panel). The membrane was simultaneously incubated with either pair of antibodies to allow a more direct comparison of protein amounts. 40S, small ribosomal subunit. ( D ) Polysomes were extracted as in (A) and hnRNP C-bound complexes were immunoprecipitated using antibodies to hnRNP C or IgG as control, followed by incubation with biotin-conjugated puromycin to label nascent polypeptide chains. 5% of polysome pellet and 100% of hnRNP C IP were then subjected to immunoblot analysis using anti-hnRNP C and anti-RPL26, as well as streptavidin-HRP.

    Journal: Nucleic Acids Research

    Article Title: Proteomic analysis of polyribosomes identifies splicing factors as potential regulators of translation during mitosis

    doi: 10.1093/nar/gkx326

    Figure Lengend Snippet: Association of hnRNP C with polysomes increases from G1 to mitosis. ( A ) MS measurements of members of the hnRNP family. Bar plot represents the logarithmic ratio of normalized MS intensities for M over G1; heatmaps reflect the relative abundance of each protein during mitosis in either ribosome-associated (‘Ribosome’) or total proteome (‘Total’) samples. ( B ) Polysomes were extracted from G1 and M cytoplasmic lysates by ultracentrifugation through a sucrose cushion, and protein content of the lysates and pellets was monitored by immunoblotting using antibodies to hnRNP C, Poly-A binding protein (PABPC1) and Ribosomal protein L26 (RPL26). ( C ) Polysomes were extracted from G1 and M cells by ultracentrifugation through a sucrose gradient, and protein content of each fraction was monitored by immunoblotting using antibodies to Ribosomal protein P0 (RPLP0) and either hnRNP C (top panel) or SRSF1 (bottom panel). The membrane was simultaneously incubated with either pair of antibodies to allow a more direct comparison of protein amounts. 40S, small ribosomal subunit. ( D ) Polysomes were extracted as in (A) and hnRNP C-bound complexes were immunoprecipitated using antibodies to hnRNP C or IgG as control, followed by incubation with biotin-conjugated puromycin to label nascent polypeptide chains. 5% of polysome pellet and 100% of hnRNP C IP were then subjected to immunoblot analysis using anti-hnRNP C and anti-RPL26, as well as streptavidin-HRP.

    Article Snippet: Secondary antibodies: HRP-conjugated anti-rabbit IgG, HRP-conjugated anti-mouse IgG, (Jackson ImmunoResearch Laboratories, 1:10 000).

    Techniques: Mass Spectrometry, Binding Assay, Incubation, Immunoprecipitation

    dCIP4 and Wsp inhibit Gbb secretion. A1–D2 , Confocal images of NMJs 6/7 stained for extracellular Gbb-GFP (red) and HRP (blue) in BG57-GAL4 /+ ( A1 , A2 ), BG57-GAL4 / UAS-gbb-GFP ( B1 , B2 ), BG57-GAL4,Df(3L)ED4342 / UAS-gbb-GFP,dcip4 1 ( C1 , C2 ), and BG57-GAL4

    Journal: The Journal of Neuroscience

    Article Title: dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal

    doi: 10.1523/JNEUROSCI.0256-10.2010

    Figure Lengend Snippet: dCIP4 and Wsp inhibit Gbb secretion. A1–D2 , Confocal images of NMJs 6/7 stained for extracellular Gbb-GFP (red) and HRP (blue) in BG57-GAL4 /+ ( A1 , A2 ), BG57-GAL4 / UAS-gbb-GFP ( B1 , B2 ), BG57-GAL4,Df(3L)ED4342 / UAS-gbb-GFP,dcip4 1 ( C1 , C2 ), and BG57-GAL4

    Article Snippet: The following antibodies were used in this study: rat anti-dCIP4 (1:1000), guinea pig anti-Wsp (a kind gift from Sven Bogdan, Universität M ̈ unster, M ̈ unster, Germany; 1:1000), rabbit anti-dynamin (a kind gift from Mani Ramaswami, Trinity College Dublin, Dublin, Ireland; 1:1000), rabbit anti-Actin (Sigma; 1:1000), rabbit anti-Myc (Cell Signaling Technology; 1:1000), mouse anti-GFP (Roche; 1:1000), and HRP-conjugated secondary antibodies (Jackson ImmunoResearch; 1:5000).

    Techniques: Staining

    A high-throughput assay (EJIPT) utilizing EJC binding to spliced mRNAs to measure splicing in vitro . Splicing reaction mixtures containing biotin-labeled pre-mRNA, 20 μM each compound, splicing extract, and 0.5 mM ATP are assembled by liquid handler in 384-well plates and incubated for 1.5 h at 30°C. Reaction mixtures are then transferred to a NeutrAvidin-coated plate, which captures biotin-labeled RNAs/RNPs postsplicing. Anti-eIF4AIII (3F1) antibody is added to detect splicing-dependent EJC formation on spliced mRNAs. Following a washing step, incubation with an HRP-conjugated anti-mouse IgG secondary antibody, and then addition of chemiluminescent substrate, signals representing eIF4AIII/mRNA complexes are obtained by an automatic plate reader.

    Journal: Molecular and Cellular Biology

    Article Title: A Quantitative High-Throughput In Vitro Splicing Assay Identifies Inhibitors of Spliceosome Catalysis

    doi: 10.1128/MCB.05788-11

    Figure Lengend Snippet: A high-throughput assay (EJIPT) utilizing EJC binding to spliced mRNAs to measure splicing in vitro . Splicing reaction mixtures containing biotin-labeled pre-mRNA, 20 μM each compound, splicing extract, and 0.5 mM ATP are assembled by liquid handler in 384-well plates and incubated for 1.5 h at 30°C. Reaction mixtures are then transferred to a NeutrAvidin-coated plate, which captures biotin-labeled RNAs/RNPs postsplicing. Anti-eIF4AIII (3F1) antibody is added to detect splicing-dependent EJC formation on spliced mRNAs. Following a washing step, incubation with an HRP-conjugated anti-mouse IgG secondary antibody, and then addition of chemiluminescent substrate, signals representing eIF4AIII/mRNA complexes are obtained by an automatic plate reader.

    Article Snippet: Plates were washed in six cycles with HNT buffer on the ELx405, and then a horseradish peroxidase (HRP)-conjugated anti-mouse IgG secondary antibody (Jackson Immunologicals) diluted 1:10,000 in HNT buffer was added and incubated for 1 h. After a final series of identical washes, 50 μl of Super Signal ELISA (enzyme-linked immunosorbent assay) Fempto chemiluminescent substrate (Pierce) was added, and luminescence signals were measured on a Perkin Elmer Envision reader.

    Techniques: High Throughput Screening Assay, Binding Assay, In Vitro, Labeling, Incubation

    Purified TDM is recognized by Mincle. (A) Chemical structure of TDM. α-Mycolate (shown), methoxy-mycolate, and keto-mycolate are the major subclasses of mycolate found in M. tuberculosis TDM. (B and C) Reporter cells were stimulated with the indicated amount of plate-coated TDM (B) or TDB (C). (D) Reporter cells were stimulated with the indicated amount of TDM, methyl α-mycolate (α-mycolate), or methyl keto-mycolate (keto-mycolate). (E) Reporter cells were stimulated with the indicated amount of TDM and TMM. (F) ELISA-based detection of TDM by Mincle-Ig. hIgG1-Fc (Ig), Mincle-Ig, and Dectin2-Ig were incubated with 0.1 nmol/0.32 cm 2 of plate-coated TDM. Bound protein was detected with anti–hIgG-HRP followed by the addition of colorimetric substrate. (G) Effect of trehalose (100 µg/ml), EDTA (10 mM), rat IgG (10 µg/ml), and anti-Mincle mAb (10 µg/ml) on TDM recognition by Mincle-Ig. ELISA-based detection was performed as in E. (H) Reporter cells were stimulated with TDM, which was treated with trehalase as described in Materials and methods. Cells were also stimulated with plate-coated anti-Mincle mAb treated with trehalase as a negative control. All data are means ± SD for triplicate assays and representative results from three independent experiments with similar results are shown.

    Journal: The Journal of Experimental Medicine

    Article Title: Direct recognition of the mycobacterial glycolipid, trehalose dimycolate, by C-type lectin Mincle

    doi: 10.1084/jem.20091750

    Figure Lengend Snippet: Purified TDM is recognized by Mincle. (A) Chemical structure of TDM. α-Mycolate (shown), methoxy-mycolate, and keto-mycolate are the major subclasses of mycolate found in M. tuberculosis TDM. (B and C) Reporter cells were stimulated with the indicated amount of plate-coated TDM (B) or TDB (C). (D) Reporter cells were stimulated with the indicated amount of TDM, methyl α-mycolate (α-mycolate), or methyl keto-mycolate (keto-mycolate). (E) Reporter cells were stimulated with the indicated amount of TDM and TMM. (F) ELISA-based detection of TDM by Mincle-Ig. hIgG1-Fc (Ig), Mincle-Ig, and Dectin2-Ig were incubated with 0.1 nmol/0.32 cm 2 of plate-coated TDM. Bound protein was detected with anti–hIgG-HRP followed by the addition of colorimetric substrate. (G) Effect of trehalose (100 µg/ml), EDTA (10 mM), rat IgG (10 µg/ml), and anti-Mincle mAb (10 µg/ml) on TDM recognition by Mincle-Ig. ELISA-based detection was performed as in E. (H) Reporter cells were stimulated with TDM, which was treated with trehalase as described in Materials and methods. Cells were also stimulated with plate-coated anti-Mincle mAb treated with trehalase as a negative control. All data are means ± SD for triplicate assays and representative results from three independent experiments with similar results are shown.

    Article Snippet: HRP-conjugated anti–human IgG (109–035-088) was from Jackson ImmunoResearch Laboratories.

    Techniques: Purification, Enzyme-linked Immunosorbent Assay, Incubation, Negative Control